Three proteins related to the hamster vaginal discharge protein aphrodisin were purified, subjected to adsorption chromatography for removal of volatile compounds and tested for pheromonal activity in an assay of copulatory behavior exhibited by male hamsters toward a surrogate female. One of the proteins is conspecific to aphrodisin, it is the second most abundant protein in the vaginal discharge. Like aphrodisin it migrates as a relatively acidic protein in electrophoresis under non-denaturing conditions, and it appears to have an identical monomeric molecular mass (17 kd) in electrophoresis with 0.1% sodium dodecylsulfate. Heterospecific proteins included the female mouse major urinary protein (MUP) and β-lactoglobulin from cow's milk, which have some similarity in amino acid sequence to aphrodisin and belong to the α2u-globulin protein superfamily. In spite of these chemical relationships, neither the conspecific protein nor the heterospecific proteins had aphrodisiac activity comparable to that of aphrodisin in the surrogate female behavioral assay. The pheromonal activity of aphrodisin thus appears to be dependent on specific structural features of the protein.
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